› 5uu1

X-ray diffraction
2Å resolution

Function and Biology Details

Reaction catalysed: 
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-183259 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine/threonine-protein kinase VRK2 Chain: A
Molecule details ›
Chain: A
Length: 324 amino acids
Theoretical weight: 36.79 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q86Y07 (Residues: 14-335; Coverage: 63%)
Gene name: VRK2
Sequence domains: Protein kinase domain
Structure domains: Transferase(Phosphotransferase) domain 1

Ligands and Environments

1 bound ligand:
Ligand 7DZ 1 x 7DZ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LNLS BEAMLINE W01B-MX2
Spacegroup: P212121
Unit cell:
a: 54.477Å b: 72.683Å c: 83.042Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.182 0.221
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Emerging roles of the αC-β4 loop in protein kinase structure, function, evolution, and disease.
Yeung et al. (2020)
1 more

1 mention without citation

Structural characterization of human Vaccinia-Related Kinases (VRK) bound to small-molecule inhibitors identifies different P-loop conformations.
Couñago et al. (2017)